ID   DMAW_ARTBC              Reviewed;         385 AA.
AC   D4AK48;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Tryptophan dimethylallyltransferase {ECO:0000305};
DE            EC=2.5.1.34 {ECO:0000250|UniProtKB:Q50EL0};
DE   AltName: Full=4-dimethylallyltryptophan synthase {ECO:0000303|PubMed:22403186};
DE            Short=DMATS {ECO:0000303|PubMed:22403186};
DE   AltName: Full=All-trans-hexaprenyl-diphosphate synthase {ECO:0000305};
DE   AltName: Full=L-tryptophan dimethylallyl transferase {ECO:0000305};
GN   Name=dmaW {ECO:0000303|PubMed:22403186}; ORFNames=ARB_04649;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
RN   [2]
RP   FUNCTION.
RX   PubMed=22403186; DOI=10.1099/mic.0.056796-0;
RA   Wallwey C., Heddergott C., Xie X., Brakhage A.A., Li S.M.;
RT   "Genome mining reveals the presence of a conserved gene cluster for the
RT   biosynthesis of ergot alkaloid precursors in the fungal family
RT   Arthrodermataceae.";
RL   Microbiology 158:1634-1644(2012).
CC   -!- FUNCTION: Tryptophan dimethylallyltransferase; part of the gene cluster
CC       that mediates the biosynthesis of fungal ergot alkaloid
CC       (PubMed:22403186). DmaW catalyzes the first step of ergot alkaloid
CC       biosynthesis by condensing dimethylallyl diphosphate (DMAP) and
CC       tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:22403186). The
CC       second step is catalyzed by the methyltransferase easF that methylates
CC       4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-
CC       methionine, resulting in the formation of 4-dimethylallyl-L-abrine
CC       (PubMed:22403186). The catalase easC and the FAD-dependent
CC       oxidoreductase easE then transform 4-dimethylallyl-L-abrine to
CC       chanoclavine-I which is further oxidized by easD in the presence of
CC       NAD(+), resulting in the formation of chanoclavine-I aldehyde
CC       (PubMed:22403186). Chanoclavine-I aldehyde is the precursor of
CC       ergoamides and ergopeptines in Clavicipitaceae, and clavine-type
CC       alcaloids such as fumiclavine in Trichocomaceae (PubMed:22403186).
CC       However, the metabolites downstream of chanoclavine-I aldehyde in
CC       Arthrodermataceae have not been identified yet (PubMed:22403186).
CC       {ECO:0000269|PubMed:22403186}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dimethylallyl diphosphate + L-tryptophan = 4-(3-methylbut-2-
CC         enyl)-L-tryptophan + diphosphate; Xref=Rhea:RHEA:14173,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:57912,
CC         ChEBI:CHEBI:58209; EC=2.5.1.34;
CC         Evidence={ECO:0000250|UniProtKB:Q50EL0};
CC   -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC       {ECO:0000305|PubMed:22403186}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q50EL0}.
CC   -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; ABSU01000001; EFE37121.1; -; Genomic_DNA.
DR   RefSeq; XP_003017766.1; XM_003017720.1.
DR   AlphaFoldDB; D4AK48; -.
DR   SMR; D4AK48; -.
DR   STRING; 663331.D4AK48; -.
DR   EnsemblFungi; EFE37121; EFE37121; ARB_04649.
DR   GeneID; 9522612; -.
DR   KEGG; abe:ARB_04649; -.
DR   eggNOG; ENOG502S2XP; Eukaryota.
DR   HOGENOM; CLU_037431_0_0_1; -.
DR   OMA; EPQVYFT; -.
DR   UniPathway; UPA00327; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0004659; F:prenyltransferase activity; IEA:UniProt.
DR   GO; GO:0050364; F:tryptophan dimethylallyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0035835; P:indole alkaloid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd13929; PT-DMATS_CymD; 1.
DR   InterPro; IPR033964; Aro_prenylTrfase.
DR   InterPro; IPR017795; Aro_prenylTrfase_DMATS.
DR   PANTHER; PTHR40627; PTHR40627; 1.
DR   Pfam; PF11991; Trp_DMAT; 1.
DR   SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1.
DR   TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
PE   3: Inferred from homology;
KW   Alkaloid metabolism; Reference proteome; Transferase.
FT   CHAIN           1..385
FT                   /note="Tryptophan dimethylallyltransferase"
FT                   /id="PRO_0000439101"
FT   BINDING         83..84
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         92
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         193
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         246
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         263
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         345
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         347
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
SQ   SEQUENCE   385 AA;  43944 MW;  4111566A477031F9 CRC64;
     MGSIEIPNCS GSIVYKTISD FIDFPNHEQK LWWHSTAPMF AEMLRVAGYD LHSQYKILGI
     FLNHVIPFLG VYPTRINNRW LSILTRYGTP FELSLNCSQS LVRYTYEPIN SATGTVKDPF
     NTHSIWDALD RLMPLQKGID LEFFKHLKQD LTVDDQDSAY LLENNLVGGQ IRTQNKLALD
     LKGGNFVLKT YIYPALKALA TGKSIKTLMF DSVYRLCRQN PSLEAPLRAL EEYVDSKGPN
     STASPRLLSC DLIDPSKSRV KIYILELNVT LEAMEDLWTM GGRLNDASTL AGLEMLRELW
     DLIKLPPGMR EYPEPFLQLG TIPDEQLPLM ANYTLHHDQA MPEPQVYFTT FGLNDGRIAD
     GLVTFFERRG WNHMAQTYKD SLRAY